Echotomographic Study in the Diagnosis of the Nonfunctioning Kidney

Ja, Martínez-Piñeiro; Ja, García Conesa; Hidalgo, Luis; J, de la Peña

doi:10.1159/000474011

Cited by 1 publication

(2 citation statements)

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“…Thiosulfinates, for example, allicin (diallyl thiosulfinate), have considerable potential for application in the agricultural and food industries because of their broad-spectrum antimicrobial and pesticide activities. 1,2 As natural antibiotics, these compounds are recognized for their broad-spectrum inhibition of bacteria and fungi, including antibiotic-resistant strains such as methicillin-resistant Staphylococcus aureus. 3 Additionally, studies on their toxic effects against Culex, Aedes aegypti larvae, and root-knot nematodes have shown them to be effective plantderived insecticides.…”

Section: Introductionmentioning

confidence: 99%

“…15−17 Due to the distinctive S�O bond of the thiosulfinate structure, these compounds are more reactive than other disulfides to nucleophilic thiol groups. 2 Therefore, poor stability in an aqueous medium for both enzymatic and chemical methods is the major obstacle limiting the bioavailability of thiosulfinates. 18 Consequently, considerable effort has been given to overcome this bottleneck and allow free range to the activity of thiosulfinates, and in situ enzymatic synthesis has proved to be a promising and plausible strategy with various applications.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of Bacterial Alliinase: Resource and Substrate Stereospecificity

Liu,

Li,

Peng

et al. 2024

J. Agric. Food Chem.

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Limited alliinase resources cause difficulties in the biosynthesis of thiosulfinates (e.g., allicin), restricting their applications in the agricultural and food industries. To effectively biosynthesize thiosulfinates, this study aimed to excavate bacterial alliinase resources and elucidate their catalytic properties. Two bacterial cystathionine β-lyases (MetCs) possessing high alliinase activity (>60 U mg −1 ) toward L-(−)-alliin were identified from Allium sativum rhizosphere isolates. Metagenomic exploration revealed that cystathionine β-lyase from Bacillus cereus (BcPatB) possessed high activity toward both L-(±)-alliin and L-(+)-alliin (208.6 and 225.1 U mg −1 ), respectively. Although these enzymes all preferred L-cysteine S-conjugate sulfoxides as substrates, BcPatB had a closer phylogenetic relationship with Allium alliinases and shared several similar features with A. sativum alliinase. Interestingly, the Trp 30 Ile 31 Ala 32 Asp 33 Met 34 motif in a cuspate loop of BcPatB, especially sites 31 and 32 at the top of the motif, was modeled to locate near the sulfoxide of L-(+)-alliin and is important for substrate stereospecificity. Moreover, the stereoselectivity and activity of mutants I31V and A32G were higher toward L-(+)-alliin than those of mutant I31L/D33E toward L-(−)-alliin. Using bacterial alliinases and chemically synthesized substrates, we obtained thiosulfinates with high antimicrobial and antinematode activities that could provide insights into the protection of crops and food.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%